Bioinformatics Analysis on Ribulose-1,5-bisphosphate Carboxylase/ Oxygenase Large Subunits in Different Plants  

Biaojin Zhang1 , Linguang Luo1 , Xiangxi Zhang1 , Ruili Li1 , Yan Song2 , Dawen Zhang1 , Yuanyuan Nie2 , Yanbing Zeng1 , Qiegen Liao1 , Yihua Wei 1
1. Institute of Quality Safety and Standards of Agricultural Products Research, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, P.R. China
2. Rice Research Institute, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, P.R. China
1. Institute of Quality Safety and Standards of Agricultural Products Research, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, P.R. China
2. Rice Research Institute, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, P.R. China
Author    Correspondence author
Molecular Plant Breeding, 2011, Vol. 2, No. 15   doi: 10.5376/mpb.2011.02.0015
Received: 29 Sep., 2011    Accepted: 20 Oct., 2011    Published: 26 Oct., 2011
© 2011 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Zhang et al., 2011, Bioinformatics Analysis on Ribulose-1,5-bisphosphate Carboxylase/ Oxygenase Large Subunits in Different Plants, Molecular Plant Breeding Vol.2 No.15 (doi: 10.5376/mpb.2011.02.0015)

Abstract

The nucleotide sequences and amino acid sequences of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunits (rbcL) from Zea mays, Arabidopsis thaliana, Pisum sativum, Citrus sinensis, Phalaenopsis aphrodite subsp. formosana, emphasizing on Oryza sativa subsp. japonica, which were registered in the Genebank, were analyzed by the tools of bioinformatics in the following aspects: the composition and the physical and chemical characteristics of nucleotide sequences and amino acid sequences, signal peptide, trans-membrane topological structure, hydrophobicity or hydrophilicity, secondary structure, sequences comparisons, and molecular systemic evolution. The results were showed as follows: the amino acid composition and characteristics of rbcLs from different higher plants were approximately identical; signal peptide and trans-membrane topological structure were not detected in the rbcLs that exhibit the traits of hydrophilic protein; the secondary structure of rbcL manly constituted with α-helix and random coil; the nucleotide sequences and amino acid sequences possess high homologies; the rbcL DNA sequence can reflect the sibships among various higher plants clearly.

Keywords
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCo); Plant; Rice (Oryza sativa L); Bioinformatics
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